ID A0A183Q369_9TREM Unreviewed; 362 AA.
AC A0A183Q369;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=ATP-grasp domain-containing protein {ECO:0000313|WBParaSite:SMTD_0002105401-mRNA-1};
GN ORFNames=SMTD_LOCUS21055 {ECO:0000313|EMBL:VDP84013.1};
OS Schistosoma mattheei.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=31246 {ECO:0000313|WBParaSite:SMTD_0002105401-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMTD_0002105401-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP84013.1, ECO:0000313|Proteomes:UP000269396}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Denwood {ECO:0000313|EMBL:VDP84013.1}, and Denwood, Zambia
RC {ECO:0000313|Proteomes:UP000269396};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl
CC phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC ChEBI:CHEBI:456216; EC=6.3.4.16;
CC Evidence={ECO:0000256|ARBA:ARBA00043687};
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DR EMBL; UZAL01046142; VDP84013.1; -; Genomic_DNA.
DR STRING; 31246.A0A183Q369; -.
DR WBParaSite; SMTD_0002105401-mRNA-1; SMTD_0002105401-mRNA-1; SMTD_0002105401.
DR Proteomes; UP000269396; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR PRINTS; PR00098; CPSASE.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Reference proteome {ECO:0000313|Proteomes:UP000269396};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 38..229
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 362 AA; 39442 MW; 88E77BA61A2B49FB CRC64;
MGGQTPNNIA MPMHRLGVPI LGTSAESIDN AENRFKFSRL LDCIGLSQPR WKELTDIDSA
KAFCEEVGYP CLVRPSYVLS GAAMNVANDH DQLITFLTAA KNISPEHPVV ISQFILDAKE
IDVDAVAQSG RLVAMAVSEH VENAGVHSGD ATLVTPPQDL NEETLKLIKE LVRALADELE
VSGPFNLQLL AKDNRLLIIE ANLRVSRSFP FVSKTLKYDF IAAATRAILG AARDSIHPPF
DTHGSKLERL SLSKSFLEPS VNVLENTVGY VGVKVPVFSF ARLLGADVLL GVEMVSTGEV
ACFGVDRYEA YLLAQAAALC NTNGLLPKPG DNVFLSIGSY RHKLEMLPRL VKFFKYCLSS
NL
//
